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Database: UniProt
Entry: A0A1T1AV87_RHOFE
LinkDB: A0A1T1AV87_RHOFE
Original site: A0A1T1AV87_RHOFE 
ID   A0A1T1AV87_RHOFE        Unreviewed;       747 AA.
AC   A0A1T1AV87;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:OOV07991.1};
GN   ORFNames=RF819_15820 {ECO:0000313|EMBL:OOV07991.1};
OS   Rhodoferax fermentans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=28066 {ECO:0000313|EMBL:OOV07991.1, ECO:0000313|Proteomes:UP000190750};
RN   [1] {ECO:0000313|EMBL:OOV07991.1, ECO:0000313|Proteomes:UP000190750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 7819 {ECO:0000313|EMBL:OOV07991.1,
RC   ECO:0000313|Proteomes:UP000190750};
RA   Kim Y.J., Farh M.E.-A., Yang D.-C.;
RT   "Genome sequencing of Rhodoferax fermentans JCM 7819.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate)
CC       is a mediator of the stringent response that coordinates a variety of
CC       cellular activities in response to changes in nutritional abundance.
CC       {ECO:0000256|RuleBase:RU003847}.
CC   -!- SIMILARITY: Belongs to the relA/spoT family.
CC       {ECO:0000256|RuleBase:RU003847}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OOV07991.1}.
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DR   EMBL; MTJN01000002; OOV07991.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T1AV87; -.
DR   STRING; 28066.RF819_15820; -.
DR   OrthoDB; 9805041at2; -.
DR   Proteomes; UP000190750; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd04876; ACT_RelA-SpoT; 1.
DR   CDD; cd05399; NT_Rel-Spo_like; 1.
DR   CDD; cd01668; TGS_RSH; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR004811; RelA/Spo_fam.
DR   InterPro; IPR007685; RelA_SpoT.
DR   InterPro; IPR004095; TGS.
DR   InterPro; IPR012676; TGS-like.
DR   InterPro; IPR033655; TGS_RelA/SpoT.
DR   NCBIfam; TIGR00691; spoT_relA; 1.
DR   PANTHER; PTHR21262:SF31; BIFUNCTIONAL (P)PPGPP SYNTHASE_HYDROLASE SPOT; 1.
DR   PANTHER; PTHR21262; GUANOSINE-3',5'-BIS DIPHOSPHATE 3'-PYROPHOSPHOHYDROLASE; 1.
DR   Pfam; PF13291; ACT_4; 1.
DR   Pfam; PF13328; HD_4; 1.
DR   Pfam; PF04607; RelA_SpoT; 1.
DR   Pfam; PF02824; TGS; 1.
DR   SMART; SM00954; RelA_SpoT; 1.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81271; TGS-like; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS51880; TGS; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:OOV07991.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190750};
KW   Transferase {ECO:0000313|EMBL:OOV07991.1}.
FT   DOMAIN          418..479
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          676..747
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   747 AA;  81970 MW;  A600C512B14CAE44 CRC64;
     MKISEIEVTT PERSAQAVLP VVAATAQSLP EHPQALARAR AFAEPLLSCE ELDTGENTLA
     HADAVAVILK RIGGSEAMQA ASYLVYACDH LNKPQEVIAK AFGDNFAALA METTKLVRVQ
     RQARMAKATR PAVVVDTPAA QQAAAVQTEN VRKMLLAFSR DLRVVMLRLA SRLQTLRFFA
     ATKRPIPEGI AAESLQVFAP LANRLGIWEI KWEMEDLAFR FMEPDTYKQV ARLLDEKRVE
     REAHVERMRS QLEADLNANG IVAKVSGRPK HIYSIVKKMR GKSLGFEKVY DVRALRILVA
     SVPECYGALS WVHHHFTPIT EEFDDYIAKP KVNGYQSLHT VVRDAAGLPT EIQIRTQAMH
     DHAENGVAAH WAYKEAGAKG YAGVSATGAY DAKIAVLRQL LAWERDLSGV QTQDLLDDRI
     YVLTPDANIV ELPQGATVVD FAYTVHTDLG HRCRGARVDG AMVPLNTALK NGQTVEVTAA
     KEGGPSRDWL NTELGYLVSH RARTKVRAWF NALALSETIA KGREAVEKLL QREGKTALKL
     DDLAVQLGFA NATALFEDVG KDEFSLRAIE QVLRPPEAPQ FDANAPVLRK PRSGDNPSKG
     GLLVVGVDSL MTQMAKCCKP APPDAICGFV TRGKGVSVHR KDCSNLKEMV ARNGERLIEV
     EWGVARAMSG SVFPVDVAVQ AHDRQGLLRD ISEVFTKEKM NVIGVQTQSI KGIAWMTFTV
     EVSDSGRLHK VLGLVAELPG VNSARRK
//
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